mProX™ Human PAK5 Stable Cell Line
- Product Category:
- Membrane Protein Stable Cell Lines
- Subcategory:
- Kinase Cell Lines
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Published Data
Fig.1 In vitro, PAK5 stimulates the migration and invasion of CC cells.
The migration and invasion abilities were assessed through Transwell assays in HeLa and SiHa cells, with PAK5 overexpression and knockdown, respectively. A scale bar of 100 μm was employed for the figures denoted as 'g' and 'h'. The data were presented as mean ± SD based on three independent experiments. Significance levels were indicated as *, P < 0.05; **, P < 0.01; ***, P < 0.001. The Cell Counting Kit-8 (CCK-8) was used for cell counting, and siRNA control (siCtrl) and siRNA targeting PAK5 (siPAK5) were utilized.
Ref: Huo, Fu-Chun, et al. "PAK5 promotes the migration and invasion of cervical cancer cells by phosphorylating SATB1." Cell Death & Differentiation 26.6 (2019): 994-1006.
Pubmed: 30082769
DOI: 10.1038/s41418-018-0178-4
Research Highlights
Xing, Yao et al. "PAK5-mediated AIF phosphorylation inhibits its nuclear translocation and promotes breast cancer tumorigenesis." International journal of biological sciences vol. 17,5 1315-1327. 27 Mar. 2021.
Despite its association with various cancer types, the precise role of PAK5 in breast cancer has remained uncertain. This investigation uncovers a pivotal function for PAK5 in thwarting apoptosis by impeding AIF's migration into the nucleus. In breast cancer cells, PAK5 hampers AIF release from mitochondria by modulating membrane properties, heightening the membrane potential, and phosphorylating AIF at Thr281 to hinder AIF/importin α3 complex formation, thereby curtailing AIF nuclear translocation. Functionally, this PAK5-mediated AIF phosphorylation fosters breast cancer cell proliferation and in vivo tumor growth. Remarkably, higher PAK5 and AIF levels in breast cancer correspond with unfavorable patient outcomes, emphasizing the therapeutic potential of targeting the PAK5-AIF pathway in breast cancer treatment.
Xing, Yao et al. "PAK5-mediated AIF phosphorylation inhibits its nuclear translocation and promotes breast cancer tumorigenesis." International journal of biological sciences vol. 17,5 1315-1327. 27 Mar. 2021.
Pubmed:
33867848
DOI:
10.7150/ijbs.58102
L Martin, Heather. et al. "Affimer-mediated locking of p21-activated kinase 5 in an intermediate activation state results in kinase inhibition." Cell reports, 2023.
Kinases are significant targets for therapeutic purposes and their inhibitors are categorized based on their mechanism of action, ranging from blocking ATP binding to covalent inhibition. A new method of inhibition is proposed by utilizing an Affimer, which binds to the P+1 pocket of p21-activated kinase 5 (PAK5) and captures it in an intermediate state of activation. PAK5 was identified through a non-hypothesis-driven high-content imaging RNAi screen in urothelial cancer cells. Its suppression led to reduced cell number, G1/S arrest, and enlarged cells, underscoring its role in the survival and proliferation of the urothelial cancer cell line. Affimer reagents were used to identify the mode of inhibition, and PAK5-Af17 was found to mimic the effects of siRNA. Co-crystallization revealed that PAK5-Af17 binds to the P+1 pocket, causing the kinase to be partially activated. This novel mechanism of inhibition highlights the potential for a new class of kinase inhibitors.
L Martin, Heather. et al. "Affimer-mediated locking of p21-activated kinase 5 in an intermediate activation state results in kinase inhibition." Cell reports, 2023.
Pubmed:
37776520
DOI:
10.1016/j.celrep.2023.113184